IN SITU STUDY of GOLD FUNCTIONALIZATION SURFACE for PROTEIN IMMOBILIZATION

Detalhes bibliográficos
Autor(a) principal: dos Santos, Adriano [UNESP]
Data de Publicação: 2014
Outros Autores: Ribeiro, Willian Campos [UNESP], Bueno, Paulo Roberto [UNESP]
Tipo de documento: Artigo
Idioma: por
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.26850/1678-4618EQJ.V39.1.2014.P244-256
http://hdl.handle.net/11449/233723
Resumo: The SAM approach for biological material immobilization is currently used in biosensors devices, for analytical and protein affinity studies. This paper focuses on the study of real time SAM formation consisted of mixed SAM of 11-mercaptoundecanoic acid (MUA) and 6-mercapto-1-hexanol, in a molar ratio of 1:3, on gold surface, by QCM-D and cyclic voltammetry techniques. It was confirmed that the SAM is a packed film, with high degree of surface coverage. As an example of protein adsorption on the SAM, it was studied, by QCM-D technique, the adsorption process of gelatin. The results demonstrate that the adsorption and coverage processes occur in a single step, resulting in the formation of a protein monolayer. This is an interesting result since it partially assures the use of Langmuir isotherm model to study protein affinity and analytical responses.
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spelling IN SITU STUDY of GOLD FUNCTIONALIZATION SURFACE for PROTEIN IMMOBILIZATIONESTUDO in SITU DA FUNCIONALIZAÇÃO DE SUPERFÍCIE DE OURO PARA IMOBILIZAÇÃO DE PROTEÍNAProtein adsorptionQCM-DSAMThe SAM approach for biological material immobilization is currently used in biosensors devices, for analytical and protein affinity studies. This paper focuses on the study of real time SAM formation consisted of mixed SAM of 11-mercaptoundecanoic acid (MUA) and 6-mercapto-1-hexanol, in a molar ratio of 1:3, on gold surface, by QCM-D and cyclic voltammetry techniques. It was confirmed that the SAM is a packed film, with high degree of surface coverage. As an example of protein adsorption on the SAM, it was studied, by QCM-D technique, the adsorption process of gelatin. The results demonstrate that the adsorption and coverage processes occur in a single step, resulting in the formation of a protein monolayer. This is an interesting result since it partially assures the use of Langmuir isotherm model to study protein affinity and analytical responses.UNESP Instituto de Química, Rua Prof. Francisco Degni n° 55UNESP Instituto de Química, Rua Prof. Francisco Degni n° 55Universidade Estadual Paulista (UNESP)dos Santos, Adriano [UNESP]Ribeiro, Willian Campos [UNESP]Bueno, Paulo Roberto [UNESP]2022-05-01T09:47:25Z2022-05-01T09:47:25Z2014-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article244-256http://dx.doi.org/10.26850/1678-4618EQJ.V39.1.2014.P244-256Ecletica Quimica, v. 39, n. 1, p. 244-256, 2014.1678-46180100-4670http://hdl.handle.net/11449/23372310.26850/1678-4618EQJ.V39.1.2014.P244-2562-s2.0-85117593765Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPporEcletica Quimicainfo:eu-repo/semantics/openAccess2022-05-01T09:47:25Zoai:repositorio.unesp.br:11449/233723Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462022-05-01T09:47:25Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv IN SITU STUDY of GOLD FUNCTIONALIZATION SURFACE for PROTEIN IMMOBILIZATION
ESTUDO in SITU DA FUNCIONALIZAÇÃO DE SUPERFÍCIE DE OURO PARA IMOBILIZAÇÃO DE PROTEÍNA
title IN SITU STUDY of GOLD FUNCTIONALIZATION SURFACE for PROTEIN IMMOBILIZATION
spellingShingle IN SITU STUDY of GOLD FUNCTIONALIZATION SURFACE for PROTEIN IMMOBILIZATION
dos Santos, Adriano [UNESP]
Protein adsorption
QCM-D
SAM
title_short IN SITU STUDY of GOLD FUNCTIONALIZATION SURFACE for PROTEIN IMMOBILIZATION
title_full IN SITU STUDY of GOLD FUNCTIONALIZATION SURFACE for PROTEIN IMMOBILIZATION
title_fullStr IN SITU STUDY of GOLD FUNCTIONALIZATION SURFACE for PROTEIN IMMOBILIZATION
title_full_unstemmed IN SITU STUDY of GOLD FUNCTIONALIZATION SURFACE for PROTEIN IMMOBILIZATION
title_sort IN SITU STUDY of GOLD FUNCTIONALIZATION SURFACE for PROTEIN IMMOBILIZATION
author dos Santos, Adriano [UNESP]
author_facet dos Santos, Adriano [UNESP]
Ribeiro, Willian Campos [UNESP]
Bueno, Paulo Roberto [UNESP]
author_role author
author2 Ribeiro, Willian Campos [UNESP]
Bueno, Paulo Roberto [UNESP]
author2_role author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (UNESP)
dc.contributor.author.fl_str_mv dos Santos, Adriano [UNESP]
Ribeiro, Willian Campos [UNESP]
Bueno, Paulo Roberto [UNESP]
dc.subject.por.fl_str_mv Protein adsorption
QCM-D
SAM
topic Protein adsorption
QCM-D
SAM
description The SAM approach for biological material immobilization is currently used in biosensors devices, for analytical and protein affinity studies. This paper focuses on the study of real time SAM formation consisted of mixed SAM of 11-mercaptoundecanoic acid (MUA) and 6-mercapto-1-hexanol, in a molar ratio of 1:3, on gold surface, by QCM-D and cyclic voltammetry techniques. It was confirmed that the SAM is a packed film, with high degree of surface coverage. As an example of protein adsorption on the SAM, it was studied, by QCM-D technique, the adsorption process of gelatin. The results demonstrate that the adsorption and coverage processes occur in a single step, resulting in the formation of a protein monolayer. This is an interesting result since it partially assures the use of Langmuir isotherm model to study protein affinity and analytical responses.
publishDate 2014
dc.date.none.fl_str_mv 2014-01-01
2022-05-01T09:47:25Z
2022-05-01T09:47:25Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.26850/1678-4618EQJ.V39.1.2014.P244-256
Ecletica Quimica, v. 39, n. 1, p. 244-256, 2014.
1678-4618
0100-4670
http://hdl.handle.net/11449/233723
10.26850/1678-4618EQJ.V39.1.2014.P244-256
2-s2.0-85117593765
url http://dx.doi.org/10.26850/1678-4618EQJ.V39.1.2014.P244-256
http://hdl.handle.net/11449/233723
identifier_str_mv Ecletica Quimica, v. 39, n. 1, p. 244-256, 2014.
1678-4618
0100-4670
10.26850/1678-4618EQJ.V39.1.2014.P244-256
2-s2.0-85117593765
dc.language.iso.fl_str_mv por
language por
dc.relation.none.fl_str_mv Ecletica Quimica
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 244-256
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
_version_ 1799964575467044864